RNase P

From Proteopedia

Yeast RNase P bound to pre-tRNA (PDB entry 6ah3) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function RNase P is a ribonuclease that processes the 5′ end of pre-transfer RNAs as well as other RNA molecules.[1]. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein (RNP) complexes; however, a few protein-only RNase Ps have been described.[2][3] In eukaryotes, the RNase P proteins have been found to have other roles. For example, many of the proteins are shared with a related RNase P, the small nucleolar RNase MRP, that is involved in processing ribosomal RNA.[4] In yeast, the proteins of RNase P also bind telomerase.[5] Sydney Altman shared in the 1989 Nobel Prize for his work on the catalytic properties of the RNP-based RNase P, as described here. Structural insights The active site of RNase P contains metal ions. Specifically, in the RNP-based RNase P, the ions at the active site are magnesium, and they seem to be zinc-based metallonucleases in the case of Arabidopsis proteinaceous RNase P. Articles in Proteopedia concerning RNase P include: A topic page on the RNP-based S. cerevisiae RNase P is found here

3D Structures of RNase P

Updated on 02-September-2019

Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.

RNP-based RNase P

6agb - RNP-based RNase P - S. cerevisiae
6ah3 - RNP-based RNase P bound to pre-tRNA substrate - S. cerevisiae

Protein-only RNase P

5diz - nuclear PRORP2 - Arabidopsis thaliana
4g23 -mitochondrial and chloroplast PRORP1 - Arabidopsis thaliana

1jox 1jp0 1u9s

2a2e 2k3r 2ki7 2vrt

3iab 3q1q 3q1r

4g23 4g24 4g25 4g26 4xgl

4xgm

5diz 5xtm

6ahv 6bv5 6bv6 6bv8 6bv9

1a6f 1d6t 1nz0 1oqk 1ts9 1tsf 1v76 1v77 1x0t

2av5 2czv 2k3r 2ki7 2ljp 2zae

3dhs 3iab 3q1q 3q1r 3wyz 3wz0

4g23 4g24 4g25 4g26 4jg4 4xgl 4xgm

5diz 5ft9

6agb 6ah3 6ahr 6ahu 6ahv 6bv5 6bv6 6bv8 6bv9 6cqc 6cwx 6d1r 6k0a 6k0b 6max

See Also

• Ribozyme
• Transfer RNA (tRNA)
• The Ribosome
• Ribonuclease

References

1. ↑ Jarrous N. Roles of RNase P and Its Subunits. Trends Genet. 2017 Sep;33(9):594-603. doi: 10.1016/j.tig.2017.06.006. Epub 2017, Jul 8. PMID:28697848 doi:http://dx.doi.org/10.1016/j.tig.2017.06.006
2. ↑ Gobert A, Pinker F, Fuchsbauer O, Gutmann B, Boutin R, Roblin P, Sauter C, Giege P. Structural insights into protein-only RNase P complexed with tRNA. Nat Commun. 2013;4:1353. doi: 10.1038/ncomms2358. PMID:23322041 doi:http://dx.doi.org/10.1038/ncomms2358
3. ↑ Engelke DR, Fierke CA. The evolution of RNase P. RNA. 2015 Apr;21(4):517-8. doi: 10.1261/rna.050732.115. PMID:25780121 doi:http://dx.doi.org/10.1261/rna.050732.115
4. ↑ Davila Lopez M, Rosenblad MA, Samuelsson T. Conserved and variable domains of RNase MRP RNA. RNA Biol. 2009 Jul;6(3):208-20. Epub 2009 Jul 30. PMID:19395864
5. ↑ Lemieux B, Laterreur N, Perederina A, Noel JF, Dubois ML, Krasilnikov AS, Wellinger RJ. Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP. Cell. 2016 May 19;165(5):1171-1181. doi: 10.1016/j.cell.2016.04.018. Epub 2016, May 5. PMID:27156450 doi:http://dx.doi.org/10.1016/j.cell.2016.04.018